Version 5.4
Mus musculus Protein: Ap2a1
Summary
InnateDB Protein IDBP-628101.2
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Ap2a1
Protein Name adaptor protein complex AP-2, alpha 1 subunit
Synonyms Adtaa;
Species Mus musculus
Ensembl Protein ENSMUSP00000127497
InnateDB Gene IDBG-180315 (Ap2a1)
Protein Structure
UniProt Annotation
Function Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin- coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 alpha subunit binds polyphosphoinositide-containing lipids, positioning AP-2 on the membrane. The AP-2 alpha subunit acts via its C- terminal appendage domain as a scaffolding platform for endocytic accessory proteins. The AP-2 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif (By similarity). {ECO:0000250}.
Subcellular Localization Cell membrane {ECO:0000250}. Membrane, coated pit {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=AP-2 appears to be excluded from internalizing CCVs and to disengage from sites of endocytosis seconds before internalization of the nascent CCV. {ECO:0000250}.
Disease Associations
Tissue Specificity Isoform A is expressed only in neuronal tissue and skeletal muscle. Isoform B is widely expressed.
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 12 experimentally validated interaction(s) in this database.
They are also associated with 40 interaction(s) predicted by orthology.
Experimentally validated
Total 12 [view]
Protein-Protein 12 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 40 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0005488 binding
GO:0005515 protein binding
GO:0008022 protein C-terminus binding
GO:0008565 protein transporter activity
Biological Process
GO:0006886 intracellular protein transport
GO:0006897 endocytosis
GO:0015031 protein transport
GO:0016192 vesicle-mediated transport
GO:1900126 negative regulation of hyaluronan biosynthetic process
Cellular Component
GO:0005905 coated pit
GO:0016020 membrane
GO:0016323 basolateral plasma membrane
GO:0016324 apical plasma membrane
GO:0030117 membrane coat
GO:0030131 clathrin adaptor complex
GO:0030141 secretory granule
Protein Structure and Domains
PDB ID MGI:101921
InterPro IPR002553 Clathrin/coatomer adaptor, adaptin-like, N-terminal
IPR003164 Clathrin adaptor, alpha-adaptin, appendage, C-terminal subdomain
IPR008152 Clathrin adaptor, alpha/beta/gamma-adaptin, appendage, Ig-like subdomain
IPR009028 Coatomer/calthrin adaptor appendage, C-terminal subdomain
IPR013041 Coatomer/clathrin adaptor appendage, Ig-like subdomain
IPR016024 Armadillo-type fold
IPR017104 Adaptor protein complex AP-2, alpha subunit
PFAM PF01602
PF02296
PF02883
PRINTS
PIRSF PIRSF037091
SMART SM00809
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt P17426
PhosphoSite PhosphoSite-P17426
TrEMBL
UniProt Splice Variant
Entrez Gene 11771
UniGene Mm.6877
RefSeq
MGI ID
MGI Symbol Ap2a1
OMIM
CCDS
HPRD
IMGT
EMBL BC031433 X14971
GenPept AAH31433 CAA33096

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca